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B cells were extracted from the animal immunized with a synthetic peptide derived from human CASP3, followed by fusion with myeloma cells to generate hybridomas. The variable light and variable heavy domains of CASP3 antibody-producing hybridomas were sequenced to construct a vector for a recombinant generation. The CASP3 monoclonal antibody gene-containing vector was then transfected into cells for cultivation, and the CASP3 recombinant monoclonal antibody was isolated and purified from the cell culture supernatant using affinity chromatography. This antibody was tested for the detection of human CASP3 protein in ELISA, WB, IHC, and IF applications.
CASP3 is a protease enzyme that plays a crucial role in apoptosis. Once activated, CASP3 cleaves various cellular substrates, including structural proteins, signaling molecules, and DNA repair enzymes, resulting in the dismantling of the cell and the removal of apoptotic cells by phagocytosis. CASP3 has been shown to be involved in a wide range of physiological and pathological processes, including development, tissue homeostasis, and various diseases, such as cancer and neurodegeneration.